Effect of anaerobic environment on the glutathione transferase isoenzymatic pattern in Proteus mirabilis.
When Proteus mirabilis was cultured anaerobically in the presence of nitrate as terminal electron acceptor, a dramatic reduction of glutathione transferase production occurred. The analysis of the glutathione affinity purified materials in terms of substrate specificity, SDS-PAGE pattern, IEF pattern and immunoblotting revealed that a significantly different glutathione transferase pattern also occurred: two new glutathione transferase forms with an isoelectric point at pH 4.8 and 5.0 appeared. Their N-terminal amino acid sequence analysis as well as the ability to bind to a glutathione affinity column indicate that major differences between anaerobic and aerobic glutathione transferase forms are mainly located in the C-terminal region of the primary structure. In contrast, no significant changes occurred in the production of glutathione transferase isoenzymes when P. mirabilis was grown anaerobically in the absence of a terminal electron acceptor. These results support the idea that bacterial glutathione transferase expression is not strictly related to the absence of oxygen stress.
Allocati
N
N
Istituto di Medicina Sperimentale, Università G. D'Annunzio, Chieti, Italy. allocati@ims.unich.it
Aceto
A
A
Cellini
L
L
Masulli
M
M
Dragani
B
B
Petruzzelli
R
R
Di Ilio
C
C
D000693:Anaerobiosis; D004591:Electrophoresis, Polyacrylamide Gel; D005982:Glutathione Transferase / Q000096:biosynthesis* / Q000302:isolation & purification; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000096:biosynthesis* / Q000302:isolation & purification; D009566:Nitrates / Q000378:metabolism; D017680:Potassium Compounds / Q000378:metabolism; D011513:Proteus mirabilis / Q000201:enzymology*; D013379:Substrate Specificity
D007527:Isoenzymes; D009566:Nitrates; D017680:Potassium Compounds; D005982:Glutathione Transferase; C023844:potassium nitrate